Chemical Approach to New Conversion of Hemoprotein Function

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The reconstitution of myoglobin with an artificially created prosthetic group is a unique method for introducing a new chemical function into the protein. In this project, we proposed two approach to the reconstitutional method in order to create a new function into myoglobin. One is the modification of heme-propionate side chains, and another is the modification of heme framework. The summary of our recent results are shown as follows :1. Protein-protein complex via an artificial interface on the protein surface was constructed ; e.g.. reconstituted myoglobin - cytochrome c complex.2. Photoinduced electron transfer was monitored within the artificial protein complexes. It is a suitable model to elucidate the mechanism of the complicated electron transfer in biological systems.3. Reconstituted myoglobin exhibits peroxidase and/or peroxygenase activities upon the addition of substrate binding site on the myoglobin surface.4. The role of two heme-propionate side chains in the myoglobin was proved by new myoglobin reconstituted with the special heme lacking one of the propionates.5. It is found that myoglobin reconstituted with iron porphycene shows extremely high dioxygen affinity.The net results demonstrate that the reconstitutional method will serve as a new way in the creation of a unique functionalized hemoprotein.